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1. Full Text Phosphorylation of the α-subunit of the eukaryotic initiation factor-2 (eIF2α) reduces protein synthesis and enhances apoptosis in response to proteasome inhibition
by Jiang, Hao-Yuan and Wek, Ronald C
Journal of Biological Chemistry, ISSN 0021-9258, 04/2005, Volume 280, Issue 14, pp. 14189 - 14202
Protein ubiquitination and subsequent degradation by the proteasome are important mechanisms regulating cell cycle, growth and differentiation, and apoptosis.... 
INDUCED GENE-EXPRESSION | MESSENGER-RNA TRANSLATION | TARGETED DISRUPTION | OXIDATIVE STRESS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENDOPLASMIC-RETICULUM STRESS | WOLCOTT-RALLISON-SYNDROME | CELL-SURVIVAL | NF-KAPPA-B | MAMMALIAN-CELLS | EIF2 KINASE GCN2 | Protein Kinases - metabolism | Phosphorylation | Protein Biosynthesis | Protein Kinases - genetics | Ubiquitin - metabolism | Activating Transcription Factor 4 | Protein Subunits - metabolism | Antineoplastic Agents - metabolism | DNA-Binding Proteins - metabolism | RNA Splicing | Transcription Factor CHOP | Trans-Activators - genetics | Eukaryotic Initiation Factor-2 - metabolism | Membrane Proteins - metabolism | CCAAT-Enhancer-Binding Proteins - genetics | Nuclear Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Fibroblasts - metabolism | Protein Subunits - genetics | CCAAT-Enhancer-Binding Proteins - metabolism | Membrane Proteins - genetics | Cells, Cultured | Gene Expression Regulation | Protein-Serine-Threonine Kinases - genetics | Nuclear Proteins - metabolism | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Regulatory Factor X Transcription Factors | Mice, Knockout | Transcription Factors - metabolism | Animals | Eukaryotic Initiation Factor-2 - genetics | Trans-Activators - metabolism | Fibroblasts - cytology | Mice | Apoptosis - physiology | Proteasome Endopeptidase Complex - metabolism | Proteasome Inhibitors
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2. Full Text ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death
by Han, Jaeseok and Back, Sung Hoon and Hur, Junguk and Lin, Yu-Hsuan and Gildersleeve, Robert and Shan, Jixiu and Yuan, Celvie L and Krokowski, Dawid and Wang, Shiyu and Hatzoglou, Maria and Kilberg, Michael S and Sartor, Maureen A and Kaufman, Randal J
Nature Cell Biology, ISSN 1465-7392, 05/2013, Volume 15, Issue 5, pp. 481 - 490
Protein misfolding in the endoplasmic reticulum (ER) leads to cell death through PERK-mediated phosphorylation of eIF2 alpha, although the mechanism is not... 
APOPTOSIS | OXIDATIVE STRESS | IN-VITRO | GENE | PHOSPHORYLATION | CHOP | ENDOPLASMIC-RETICULUM STRESS | MICE LACKING | TRANSLATIONAL CONTROL | ATF4 | CELL BIOLOGY | Transcription Factor CHOP - genetics | Phosphorylation | Protein Biosynthesis | Reactive Oxygen Species - metabolism | RNA, Messenger - metabolism | Chromatin Immunoprecipitation | Adenosine Triphosphate - metabolism | Cell Death | Eukaryotic Initiation Factor-2 - metabolism | Transcription, Genetic | Binding Sites | Promoter Regions, Genetic | Cell Survival | RNA, Messenger - genetics | Gene Expression Regulation | Activating Transcription Factor 4 - genetics | Unfolded Protein Response | Protein Folding | Protein Interaction Mapping | Animals | Activating Transcription Factor 4 - metabolism | Endoplasmic Reticulum Stress | Eukaryotic Initiation Factor-2 - genetics | Protein Binding | Mice | Transcription Factor CHOP - metabolism | Autophagy (Cytology) | Protein folding | Cellular control mechanisms | Genetic aspects | Research | Properties | Observations | Endoplasmic reticulum
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3. Full Text Endogenous siRNAs from naturally formed dsRNAs regulate transcripts in mouse oocytes
by Watanabe, Toshiaki and Totoki, Yasushi and Toyoda, Atsushi and Kaneda, Masahiro and Kuramochi-Miyagawa, Satomi and Obata, Yayoi and Chiba, Hatsune and Kohara, Yuji and Kono, Tomohiro and Nakano, Toru and Surani, M. Azim and Sakaki, Yoshiyuki and Sasaki, Hiroyuki
Nature, ISSN 0028-0836, 05/2008, Volume 453, Issue 7194, pp. 539 - 543
RNA interference (RNAi) is a mechanism by which doublestranded RNAs (dsRNAs) suppress specific transcripts in a sequence-dependent manner. dsRNAs are processed... 
GERMLINE | SMALL RNAS | GENE | RETROTRANSPOSON | MULTIDISCIPLINARY SCIENCES | ANTISENSE | C-ELEGANS | TESTES | MICRORNAS | GENOME | PIWI | RNA, Small Interfering - genetics | Molecular Sequence Data | RNA, Messenger - metabolism | Retroelements - genetics | Eukaryotic Initiation Factor-2 - deficiency | Pseudogenes - genetics | RNA Interference | Gene Expression Regulation, Developmental | Polymerase Chain Reaction | Eukaryotic Initiation Factor-2 - metabolism | Female | RNA, Double-Stranded - metabolism | Oocytes - growth & development | Ribonuclease III - genetics | Ribonuclease III - metabolism | Gene Library | Oocytes - metabolism | Mice, Inbred C57BL | RNA, Messenger - genetics | Ribonuclease III - deficiency | Animals | Eukaryotic Initiation Factor-2 - genetics | RNA, Double-Stranded - genetics | Argonaute Proteins | Mice | RNA, Small Interfering - metabolism | Genetic aspects | RNA | Properties | Oocytes | Life sciences | Ribonucleic acid--RNA | Genes | Rodents
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4. Full Text A dicer-independent miRNA biogenesis pathway that requires Ago catalysis
by Chong, Mark M. W and Dos Santos, Camila O and Cheloufi, Sihem and Hannon, Gregory J
Nature, ISSN 0028-0836, 06/2010, Volume 465, Issue 7298, pp. 584 - 589
The nucleolytic activity of animal Argonaute proteins is deeply conserved, despite its having no obvious role in microRNA-directed gene regulation. In mice,... 
RISC | SMALL RNAS | SLICER | GENE | ARGONAUTE FAMILY | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | SIRNAS | MICRORNAS | RECRUITS | IDENTIFICATION | Biocatalysis | Ribonuclease III - metabolism | Molecular Sequence Data | MicroRNAs - biosynthesis | Embryo, Mammalian - metabolism | Anemia - metabolism | Homozygote | Anemia - genetics | Animals | Embryo, Mammalian - embryology | Base Sequence | Eukaryotic Initiation Factor-2 - genetics | Alleles | Argonaute Proteins | Eukaryotic Initiation Factor-2 - metabolism | Embryonic development | MicroRNA | Molecular genetics | Physiological aspects | Genetic aspects | Research | Properties | Genetic regulation | Enzyme kinetics | Proteins | Biosynthesis | Target recognition | Gene expression | Rodents
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5. Full Text The miR-144/451 locus is required for erythroid homeostasis
by Rasmussen, Kasper D and Simmini, Salvatore and Abreu-Goodger, Cei and Bartonicek, Nenad and Di Giacomo, Monica and Bilbao-Cortes, Daniel and Horos, Rastislav and von Lindern, Marieke and Enright, Anton J and O'Carroll, Dónal
Journal of experimental medicine, ISSN 0022-1007, 2010, Volume 207, Issue 7, pp. 1351 - 1358
The process of erythropoiesis must be efficient and robust to supply the organism with red bloods cells both under condition of homeostasis and stress. The... 
MEDICINE, RESEARCH & EXPERIMENTAL | PROGENITORS | C-KIT | RECEPTOR | MICE | IMMUNOLOGY | MICRORNA | Hyperplasia | Mice, Inbred C57BL | Erythroblasts - metabolism | Erythroid Cells - metabolism | Genetic Loci - genetics | Anemia - pathology | MicroRNAs - metabolism | Cell Differentiation - genetics | Anemia - genetics | Animals | Gene Expression Regulation, Developmental | Eukaryotic Initiation Factor-2 - genetics | Argonaute Proteins | Eukaryotic Initiation Factor-2 - metabolism | Erythroid Cells - pathology | Mice | MicroRNAs - genetics | Cell Lineage - genetics | Homeostasis - genetics | Erythroblasts - pathology | Erythropoiesis - genetics | Brief Definitive Report
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6. Full Text Phosphorylation of eIF2 facilitates ribosomal bypass of an inhibitory upstream ORF to enhance CHOP translation
by Palam, Lakshmi Reddy and Baird, Thomas D and Wek, Ronald C
Journal of Biological Chemistry, ISSN 0021-9258, 04/2011, Volume 286, Issue 13, pp. 10939 - 10949
In response to different environmental stresses, phosphorylation of eukaryotic initiation factor-2 (eIF2) rapidly reduces protein synthesis, which lowers... 
MESSENGER-RNAS | OXIDATIVE STRESS | UNFOLDED PROTEIN RESPONSE | OPEN READING FRAMES | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | GENE-EXPRESSION | EUKARYOTIC INITIATION-FACTOR-2 | ENDOPLASMIC-RETICULUM STRESS | REINITIATION | MAMMALIAN-CELLS | Open Reading Frames - physiology | Phosphorylation - physiology | Stress, Physiological - physiology | Cell Line | Transcription Factor CHOP - genetics | RNA, Messenger - genetics | Protein Biosynthesis - physiology | Activating Transcription Factor 4 - genetics | Ribosomes - metabolism | RNA, Messenger - metabolism | Animals | Activating Transcription Factor 4 - metabolism | Ribosomes - genetics | Eukaryotic Initiation Factor-2 - genetics | Eukaryotic Initiation Factor-2 - metabolism | Mice | Apoptosis - physiology | Transcription Factor CHOP - biosynthesis | Translation | Protein Synthesis | ER Stress | Translation Regulation | Translation Control | Protein Synthesis and Degradation
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7. Full Text A Novel miRNA Processing Pathway Independent of Dicer Requires Argonaute2 Catalytic Activity
by Daniel Cifuentes and Huiling Xue and David W. Taylor and Heather Patnode and Yuichiro Mishima and Sihem Cheloufi and Enbo Ma and Shrikant Mane and Gregory J. Hannon and Nathan D. Lawson and Scot A. Wolfe and Antonio J. Giraldez
Science, ISSN 0036-8075, 6/2010, Volume 328, Issue 5986, pp. 1694 - 1698
Dicer is a central enzyme in microRNA (miRNA) processing. We identified a Dicer-independent miRNA biogenesis pathway that uses Argonaute2 (Ago2) slicer... 
Morphogenesis | MicroRNA | Messenger RNA | RNA | REPORTS | Erythrocytes | Stem cells | Catalytic activity | Nucleotides | Embryos | Sequencing | RNA CLEAVAGE | ZEBRAFISH | SLICER | MULTIDISCIPLINARY SCIENCES | PASSENGER-STRAND | SIRNAS | SHRNAS | ZINC-FINGER NUCLEASES | DROSOPHILA | Erythropoiesis | Recombinant Proteins - metabolism | Biocatalysis | Ribonuclease III - metabolism | RNA Processing, Post-Transcriptional | Zebrafish Proteins - metabolism | Humans | Embryo, Nonmammalian - metabolism | MicroRNAs - metabolism | Embryonic Development | Zebrafish - embryology | Zebrafish - genetics | Animals | Models, Biological | Eukaryotic Initiation Factor-2 - genetics | Zebrafish - metabolism | Argonaute Proteins | Eukaryotic Initiation Factor-2 - metabolism | RNA Precursors - metabolism | Zebrafish Proteins - genetics | Nucleic Acid Conformation | MicroRNAs - chemistry | Physiological aspects | Enzymes | Genetic aspects | Research | Gene mutations
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8. Full Text Conserved vertebrate mir-451 provides a platform for Dicer-independent, Ago2-mediated microRNA biogenesis
by Jr-Shiuan Yang and Thomas Maurin and Nicolas Robine and Kasper D. Rasmussen and Kate L. Jeffrey and Rohit Chandwani and Eirini P. Papapetrou and Michel Sadelain and Donal O'Carroll and Eric C. Lai and Gary Ruvkun
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2010, Volume 107, Issue 34, pp. 15163 - 15168
Canonical animal microRNAs (miRNAs) are generated by sequential cleavage of precursor substrates by the Drosha and Dicer RNase III enzymes. Several variant... 
Datasets | Vertebrates | MicroRNA | RNA | Blood cells | Stem cells | HeLa cells | Gene expression regulation | Sensors | Repression | Slicer | miRNA reprogramming | Gene suppression | POSTTRANSCRIPTIONAL REGULATION | PROTEINS REVEALS | SMALL RNAS | MULTIDISCIPLINARY SCIENCES | SIRNAS | CLEAVAGE | MORPHOGENESIS | PATHWAY | gene suppression | MOUSE OOCYTES | EXPRESSION | ARGONAUTE2 | RNA, Small Interfering - genetics | MicroRNAs - antagonists & inhibitors | Humans | Molecular Sequence Data | DNA Primers - genetics | Eukaryotic Initiation Factor-2 - deficiency | Base Sequence | Conserved Sequence | Eukaryotic Initiation Factor-2 - metabolism | DEAD-box RNA Helicases - metabolism | Nucleic Acid Conformation | Mutagenesis, Site-Directed | Ribonuclease III - metabolism | Endoribonucleases - metabolism | Mice, Inbred C57BL | MicroRNAs - biosynthesis | Sequence Homology, Nucleic Acid | Mice, Knockout | Animals | Eukaryotic Initiation Factor-2 - genetics | Argonaute Proteins | Mice | MicroRNAs - genetics | HeLa Cells | MicroRNAs - chemistry | Growth | Biosynthesis | Genetic aspects | Research | Properties | Genetic regulation | Enzymes | Gene silencing | miRNA | Argonaute 2 protein | Ribonuclease III | Biological Sciences
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9. Full Text DNA immunization with eukaryotic initiation factor-2α of Toxoplasma gondii induces protective immunity against acute and chronic toxoplasmosis in mice
by Chen, Jia and Huang, Si-Yang and Zhou, Dong-Hui and Li, Zhong-Yuan and Petersen, Eskild and Song, Hui-Qun and Zhu, Xing-Quan
Vaccine, ISSN 0264-410X, 2013, Volume 31, Issue 52, pp. 6225 - 6231
Highlights • Vaccination with Toxoplasma gondii IF2α DNA vaccine induced specific humoral and cellular responses. • Significant production of IFN-γ and IL-2... 
Allergy and Immunology | DNA vaccine | Eukaryotic initiation factor-2α (TgIF2α) | Mice | Toxoplasma gondii | Protective immunity | Toxoplasmosis | MEDICINE, RESEARCH & EXPERIMENTAL | Eukaryotic initiation factor-2 alpha (TgIF2 alpha) | IFN-GAMMA | VACCINE | PLASMID | IMMUNOLOGY | PERFORIN-LIKE PROTEIN-1 | CD8(+) T-CELLS | RESPONSES | CD4(+) | INFECTION | PARASITE | Toxoplasma - immunology | Vaccines, DNA - genetics | Virulence Factors - genetics | Immunoglobulin G - blood | Vaccines, DNA - immunology | Virulence Factors - immunology | Protozoan Proteins - genetics | Th1 Cells - immunology | Toxoplasmosis, Animal - prevention & control | Vaccines, DNA - administration & dosage | CD4-Positive T-Lymphocytes - immunology | Antibodies, Protozoan - blood | Toxoplasmosis, Animal - parasitology | Female | Brain - parasitology | Disease Models, Animal | Protozoan Vaccines - genetics | Protozoan Vaccines - immunology | Interferon-gamma - secretion | Injections, Intramuscular | Protozoan Vaccines - administration & dosage | Animals | Toxoplasma - genetics | Eukaryotic Initiation Factor-2 - genetics | Survival Analysis | Toxoplasmosis, Animal - immunology | Brain - pathology | CD8-Positive T-Lymphocytes - immunology | Eukaryotic Initiation Factor-2 - immunology | Interleukin-2 - secretion | Protozoan Proteins - immunology | Toxoplasmosis, Animal - pathology
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10. Full Text Switching from Repression to Activation: MicroRNAs Can Up-Regulate Translation
by Shobha Vasudevan and Yingchun Tong and Joan A. Steitz
Science, ISSN 0036-8075, 12/2007, Volume 318, Issue 5858, pp. 1931 - 1934
AU-rich elements (AREs) and microRNA target sites are conserved sequences in messenger RNA (mRNA) 3′ untranslated regions (3′UTRs) that control gene expression... 
Up regulation | Cell growth | Starvation | MicroRNA | Messenger RNA | HEK293 cells | Cell cycle | HeLa cells | Reports | Repression | Three prime untranslated regions | MESSENGER-RNA DEGRADATION | SIRNAS | MIRNAS | MULTIDISCIPLINARY SCIENCES | RNA-Binding Proteins - genetics | Up-Regulation | Protein Biosynthesis | Cell Proliferation | Humans | Tumor Necrosis Factor-alpha - genetics | MicroRNAs - metabolism | RNA, Messenger - metabolism | Transfection | HMGA2 Protein - genetics | Eukaryotic Initiation Factor-2 - metabolism | 3' Untranslated Regions | Cell Line | Interphase | RNA, Messenger - genetics | Computational Biology | Gene Expression Regulation | Ribonucleoproteins - metabolism | Base Pairing | Cell Cycle | Eukaryotic Initiation Factor-2 - genetics | Argonaute Proteins | HeLa Cells | Tumor Necrosis Factor-alpha - biosynthesis | RNA-Binding Proteins - metabolism | Research | DNA binding proteins | Nucleotides | RNA | Genetic translation | Proteins | Signal transduction | Cellular biology | Ribonucleic acid | Molecular biology | Gene expression | Ribonucleic acid--RNA
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11. Full Text Cytoplasmic STAT3 Represses Autophagy by Inhibiting PKR Activity
by Shen, Shensi and Niso-Santano, Mireia and Adjemian, Sandy and Takehara, Tetsuo and Malik, Shoaib Ahmad and Minoux, Hervé and Souquere, Sylvie and Mariño, Guillermo and Lachkar, Sylvie and Senovilla, Laura and Galluzzi, Lorenzo and Kepp, Oliver and Pierron, Gérard and Maiuri, Maria Chiara and Hikita, Hayato and Kroemer, Guido and Kroemer, Romano
Molecular Cell, ISSN 1097-2765, 12/2012, Volume 48, Issue 5, pp. 667 - 680
In a screen designed to identify novel inducers of autophagy, we discovered that STAT3 inhibitors potently stimulate the autophagic flux. Accordingly, genetic... 
CELLS | ACTIVATION | MITOCHONDRIAL STAT3 | PROTEIN | SIGNALING PATHWAY | INFLAMMATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | DIMERIZATION | KAPPA-B | INTEGRATED STRESS-RESPONSE | UNPHOSPHORYLATED STAT3 | CELL BIOLOGY | Palmitic Acid - pharmacology | Phosphorylation | eIF-2 Kinase - metabolism | Humans | Male | STAT3 Transcription Factor - chemistry | Recombinant Fusion Proteins - metabolism | Autophagy - drug effects | Eukaryotic Initiation Factor-2 - deficiency | Transfection | RNA Interference | Time Factors | STAT3 Transcription Factor - deficiency | Eukaryotic Initiation Factor-2 - metabolism | Protein Interaction Domains and Motifs | STAT3 Transcription Factor - genetics | STAT3 Transcription Factor - metabolism | eIF-2 Kinase - genetics | Cytoplasm - enzymology | Catalytic Domain | Signal Transduction | Mice, Inbred C57BL | eIF-2 Kinase - chemistry | Mice, Knockout | Protein Interaction Mapping | src Homology Domains | Animals | Eukaryotic Initiation Factor-2 - genetics | Cell Line, Tumor | Protein Conformation | Mice | Molecular Docking Simulation | Enzyme Activation | STAT3 Transcription Factor - antagonists & inhibitors | Fatty acids | Universities and colleges
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12. Full Text Phase Separation of C9orf72 Dipeptide Repeats Perturbs Stress Granule Dynamics
by Boeynaems, Steven and Bogaert, Elke and